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2MXQ

The solution structure of DEFA1, a highly potent antimicrobial peptide from the horse

Summary for 2MXQ
Entry DOI10.2210/pdb2mxq/pdb
NMR InformationBMRB: 25424
DescriptorPaneth cell-specific alpha-defensin 1 (1 entity in total)
Functional Keywordsantimicrobial protein
Biological sourceEquus caballus (domestic horse,equine)
Total number of polymer chains1
Total formula weight4086.81
Authors
Jung, S.,Michalek, M.,Shomali, M.,Soennichsen, F.D. (deposition date: 2015-01-12, release date: 2015-04-22, Last modification date: 2023-06-14)
Primary citationMichalek, M.,Jung, S.,Shomali, M.R.,Cauchard, S.,Sonnichsen, F.D.,Grotzinger, J.
Solution structure and functional studies of the highly potent equine antimicrobial peptide DEFA1.
Biochem.Biophys.Res.Commun., 459:668-672, 2015
Cited by
PubMed Abstract: Defensins are small effector molecules of the innate immune system that are present in almost all organisms including plants and animals. These peptides possess antimicrobial activity against a broad range of microbes including bacteria, fungi and viruses and act as endogenous antibiotics. α-Defensins are a subfamily of the defensin family and their expression is limited to specific tissues. Equine DEFA1 is an enteric α-defensin exclusively secreted by Paneth cells and shows an activity against a broad spectrum of microbes, including typical pathogens of the horse such as Rhodococcus equi, various streptococci strains, Salmonella choleraesuis, and Pasteurella multocida. Here, we report the three-dimensional structure of DEFA1 solved by NMR-spectroscopy and demonstrate its specific function of aggregating various phospholipids.
PubMed: 25769951
DOI: 10.1016/j.bbrc.2015.02.168
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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